ID TREA_PIMHY Reviewed; 585 AA.
AC Q8MMG9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 13-SEP-2023, entry version 58.
DE RecName: Full=Trehalase;
DE EC=3.2.1.28;
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE Flags: Precursor;
GN Name=tre1;
OS Pimpla hypochondriaca (Parasitoid wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Ichneumonoidea;
OC Ichneumonidae; Pimplinae; Pimplini; Pimpla.
OX NCBI_TaxID=135724;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 33-38.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12727301; DOI=10.1016/s1532-0456(03)00041-3;
RA Parkinson N.M., Conyers C.M., Keen J.N., MacNicoll A.D., Smith I.,
RA Weaver R.J.;
RT "cDNAs encoding large venom proteins from the parasitoid wasp Pimpla
RT hypochondriaca identified by random sequence analysis.";
RL Comp. Biochem. Physiol. 134C:513-520(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; AJ459958; CAD31109.1; -; mRNA.
DR AlphaFoldDB; Q8MMG9; -.
DR SMR; Q8MMG9; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR GlyCosmos; Q8MMG9; 2 sites, No reported glycans.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0005991; P:trehalose metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001661; Glyco_hydro_37.
DR InterPro; IPR018232; Glyco_hydro_37_CS.
DR PANTHER; PTHR23403; TREHALASE; 1.
DR PANTHER; PTHR23403:SF1; TREHALASE; 1.
DR Pfam; PF01204; Trehalase; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00927; TREHALASE_1; 1.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Secreted;
KW Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:12727301"
FT CHAIN 33..585
FT /note="Trehalase"
FT /id="PRO_0000230800"
FT ACT_SITE 338
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 535
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191..192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302..304
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 585 AA; 66458 MW; B991F2D9C94A2579 CRC64;
MAKTTPMAKP SVGLLTLQVL VFCALTGSLA SAGSIGHVTP RSDLCDSEVY CQGELLKTIQ
LGEVFKDGKT FVDHYQVNDP SVTVANFRKL MAETGGKPNK DQLTQYVKEN FAQENEVIDW
SPPDWQENPE FLQRVQDPVF RKWAKDLNDV WKIISRKVAP SVAEHPERHS IISVDNGFIV
PGGRFQEFYY WDSYWVMEGL LLTGMKNTSR GILENFLSMV TRFGFIPNGG RVYYLMRSQP
PLLIPMVDLY LTHTGDMQFL RDNIGTLEKE LGYFLSQKTV DVTKNGKTYK MARYIVSSNG
PRPESYREDY ELAKNINDEA EKRRFYEDLK AAAESGWDFS SRWYISENGT RGSLSNIATR
NIIPVELNAF LQRNARMLAQ FHTTLGNPTK AKYYKDIATS YQQAIDDVLW SESEGVWLDF
DLRNSQHRNY FFPTNVAPLY TQSFDSSKAQ IYGQRAAAYL TRNGILDYMG GTPASLFPTG
EQWDLPNAWP PLQSIIVQAL RNSNEESAEK LAKELAIRWL RANHKGYSQS GQMFEKYDAL
NPGKFGGGGE YVVQEGFGWT NGVVYEFLNS YPNATPDDNV HMNNN
//
